Spectrin, from human erythrocytes
Spectrin, from human erythrocytes structure
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Common Name | Spectrin, from human erythrocytes | ||
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| CAS Number | 12634-43-4 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Protection by taurine and thiotaurine against biochemical and cellular alterations induced by diabetes in a rat model.
Adv. Exp. Med. Biol. 775 , 321-43, (2013) In this study, the actions of taurine (TAU), a sulfonate, and thiotaurine (TTAU), a thiosulfonate, on diabetes-mediated biochemical alterations in red blood cells (RBCs) and plasma and on the RBC membrane, morphology and spectrin distribution were examined in... |
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[Deformability of the erythrocytes membrane in rats of different age in hypoxia].
Fiziol. Zh. 59(3) , 72-7, (2013) Using modern ("laser tweezers", low ionic strength Liss, definition of microviscosity of erythrocyte membranes by fluorescence probe pyrene) and classical methods of investigation the osmotic resistance of red blood cells and protein membrane of red blood cel... |
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Release of an ~55kDa fragment containing the actin-binding domain of β-spectrin by caspase-8 during FND-induced apoptosis depends on the presence of protein 4.1.
Arch. Biochem. Biophys. 535(2) , 205-13, (2013) Analyses of the status of the membrane spectrin-based skeleton during fludarabine/mitoxantrone/dexamethasone-induced (FND-induced) apoptosis revealed proteolytic degradation of β-spectrin, with the prevalent appearance of a specific fragment with a molecular ... |
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An open-and-shut case?
Blood 122(17) , 2928-9, (2013)
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Link up and fold up--templating the formation of spectrin tetramers.
J. Mol. Biol. 426(1) , 7-10, (2014)
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Cytoskeleton: axons earn their stripes.
Curr. Biol. 23(5) , R197-8, (2013) Axons must be supported by a strong and flexible cytoskeleton. New 'super-resolution' imaging of the submembranous axonal cytoskeleton reveals that it is organized in a periodic, ladder-like structure with alternating rings of actin linked together by interve... |
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Hereditary spherocytosis due to band 3 deficiency: 15 novel mutations in SLC4A1.
Am. J. Hematol. 88(2) , 159-60, (2013)
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The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation.
Blood 122(17) , 3045-53, (2013) Hereditary elliptocytosis (HE) and hereditary pyropoikilocytosis (HPP) are common disorders of erythrocyte shape primarily because of mutations in spectrin. The most common HE/HPP mutations are located distant from the critical αβ-spectrin tetramerization sit... |
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Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.
Phys. Chem. Chem. Phys. 15(37) , 15508-17, (2013) A deep understanding of the physicochemical factors modulating amyloid aggregation of proteins is crucial to develop therapeutic and preventive approaches for amyloid-related diseases. The earliest molecular events of the aggregation cascade represent some of... |
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Spectrin domain of eukaryotic initiation factor 3a is the docking site for formation of the a:b:i:g subcomplex.
J. Biol. Chem. 288(39) , 27951-9, (2013) eIF3a (eukaryotic translation initiation factor 3a), one of the core subunits of the eIF3 complex, has been implicated in regulating translation of different mRNAs and in tumorigenesis. A subcomplex consisting of eIF3a, eIF3b, eIF3g, and eIF3i (eIF3(a:b:i:g))... |